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onsible
ceptorntial for
only the
c factor
is synomach,
side the
highly
transcobalamin synthesis. The affected child displays few
symptoms at birth, but within months a severe deficiency
develops and, if left untreated, it leads to lifelong impairments due to neurological damage.23–27 Several different
kinds of mutations leading to a lack of transcobalamin
have been identified, including deletions and mutations
resulting in erroneous RNA editing.23–27
Haptocorrin is heavily glycosylated and is expressed in
many, but not all, mammals.28 In humans, haptocorrin is
Vitamin B12 (B12/Cobalamin)
b
Cytosol
5-methyl TH-
Folate
Homocysteine
Methionine synthase
Purines, pyrimidines
TH-
Folate
Methylcobalamin
Methionine
Mitochondrion
Methylmalonyl-CoA
Methylmalonyl-CoA
mutase
Adenosylcobalamin
Succinyl-CoA
B12 structure. The core of B12 consists of a corrin ring that encircles a
n atoms from the corrin ring, as well as to a nitrogen atom from a
ositioned below the plane of the corrin ring and a variable group (R)
able group can be occupied by several ligands, including a hydroxyl,
matically active cofactor carries either a methyl or a 5' -deoxadenosyl
efers to all variants of the vitamin, unless otherwise stated.
two distinct enzymatic processes: the conversion of homocysteine to
he 1 Nexø et al. Nat. Rev. Gastroentero. 2012, 9 (6), 345-354.
conversion of methylmalonyl-CoA to succinyl-CoA by mitochondrial
2 Russell-Jones et al. Bioconjugate Chem. 1995, 6 (1), 34-42.
inked to folate metabolism because the methyl group transferred to
3 tetrahydrofolate al. Bioconjugate Chem. 1999, 10 (6),essential
thylRussell-Jones et to tetrahydrofolate. T
etrahydrofolate is 1131-1136.